Crystallization of Glycosyltransferase, pp-GalNAc-T10(<Special Issue>Recent Research Development in Bio-Organic Materials)
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- Kubota Tomomi
- Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
Bibliographic Information
- Other Title
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- 糖転移酵素の結晶化 : pp-GalNAc-T10(<特集>バイオ・有機材料研究の最新動向)
- 糖転移酵素の結晶化--pp-GalNAc-T10
- トウ テンイ コウソ ノ ケッショウカ pp GalNAc T10
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Abstract
In post-genomic era, glycosylation involved in post-translational modification is one of the central issues in the field of bioscience. Glycosyltransferases synthesize carbohydrate chains, and their structural information is vital to understand their substrate specificities, which would further elucidate the glycosylation process in the cells. Of more than 180 glycosyltransferases identified, only a dozen were successfully crystallized. This is mainly due to the difficulty in the crystallization of enzymes. The enzymes themselves are glycosylated proteins, therefore, it is difficult to obtain a large yield of purified preparation by useful expression hosts of E. coli and yeast. Studies of carbohydrate chains in crystal growth of glyco-protein will facilitate the progress of structural determination of glycoproteins.
Journal
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- Journal of the Japanese Association for Crystal Growth
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Journal of the Japanese Association for Crystal Growth 33 (5), 375-380, 2006
The Japanese Association for Crystal Growth
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Details 詳細情報について
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- CRID
- 1390001205898355712
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- NII Article ID
- 110006154877
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- NII Book ID
- AN00188386
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- ISSN
- 21878366
- 03856275
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- NDL BIB ID
- 8630730
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- CiNii Articles
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- Abstract License Flag
- Disallowed